IGFBP5 Lentiviral Activation Particles (h): sc-400945-LAC

IGFBP5 (insulin-like growth factor binding protein 5) is a secreted and extracellular matrix–associated regulator of IGF signaling that modulates the bioavailability and receptor engagement of IGF-I and IGF-II. By shaping IGF1R-driven PI3K–AKT and MAPK/ERK pathway output, IGFBP5 influences cell proliferation, survival, migration, and differentiation, with additional IGF-independent effects on cell adhesion and matrix remodeling. In human tissues, IGFBP5 is linked to mesenchymal and fibroblast biology, osteogenic programs, and wound-repair–associated transcriptional states, often intersecting with TGF-β/SMAD signaling and ECM organization. Dysregulated IGFBP5 expression has been reported across fibrotic and tumor-associated microenvironments, making it a useful node for studying context-specific growth factor responsiveness and stromal remodeling.

IGFBP5 Lentiviral Activation Particles (h) address this need by packaging the complete synergistic activation mediator (SAM) transcriptional activation system into transduction-ready, high-titer lentiviral particles, enabling efficient IGFBP5 upregulation across a broader range of human cell types.

IGFBP5 Lentiviral Activation Particles (h) deliver all functional components of the synergistic activation mediator (SAM) system via lentiviral transduction. The system comprises three particle preparations co-transduced into target cells: one encoding catalytically inactive dCas9 (D10A and N863A mutations) fused to the VP64 transactivation domain with a blasticidin resistance gene; one encoding the MS2-p65-HSF1 fusion protein with a hygromycin resistance gene; and one encoding a target-specific 20 nt sgRNA fused to two MS2 RNA aptamers with a puromycin resistance gene. Following lentiviral transduction and genomic integration of the expression cassettes, the SAM components are stably expressed and assemble at the target locus within the proximal promoter region upstream of the IGFBP5 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous IGFBP5 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native IGFBP5 genomic locus and regulatory architecture.

The lentiviral format offers several practical advantages: stable genomic integration supports heritable activation across cell divisions; high-titer particle preparations eliminate the need for in-house viral production; and compatibility with primary, non-dividing, and transfection-resistant cell types expands experimental accessibility. Successful transduction can be confirmed and enriched through triple antibiotic selection using puromycin, hygromycin, and blasticidin.

For Research Use Only. Not Intended for Diagnostic or Therapeutic Use.